ID   MUKB_YERE8              Reviewed;        1481 AA.
AC   A1JMM2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Chromosome partition protein MukB {ECO:0000255|HAMAP-Rule:MF_01800};
DE   AltName: Full=Structural maintenance of chromosome-related protein {ECO:0000255|HAMAP-Rule:MF_01800};
GN   Name=mukB {ECO:0000255|HAMAP-Rule:MF_01800}; OrderedLocusNames=YE1556;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Plays a central role in chromosome condensation, segregation
CC       and cell cycle progression. Functions as a homodimer, which is
CC       essential for chromosome partition. Involved in negative DNA
CC       supercoiling in vivo, and by this means organize and compact
CC       chromosomes. May achieve or facilitate chromosome segregation by
CC       condensation DNA from both sides of a centrally located replisome
CC       during cell division. {ECO:0000255|HAMAP-Rule:MF_01800}.
CC   -!- SUBUNIT: Homodimerization via its hinge domain. Binds to DNA via its C-
CC       terminal region. Interacts, and probably forms a ternary complex, with
CC       MukE and MukF via its C-terminal region. The complex formation is
CC       stimulated by calcium or magnesium. Interacts with tubulin-related
CC       protein FtsZ. {ECO:0000255|HAMAP-Rule:MF_01800}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC       Rule:MF_01800}. Note=Restricted to the nucleoid region.
CC       {ECO:0000255|HAMAP-Rule:MF_01800}.
CC   -!- DOMAIN: The hinge domain, which separates the large intramolecular
CC       coiled coil regions, allows the homodimerization, forming a V-shaped
CC       homodimer. {ECO:0000255|HAMAP-Rule:MF_01800}.
CC   -!- SIMILARITY: Belongs to the SMC family. MukB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01800}.
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DR   EMBL; AM286415; CAL11634.1; -; Genomic_DNA.
DR   RefSeq; WP_005170968.1; NC_008800.1.
DR   RefSeq; YP_001005850.1; NC_008800.1.
DR   AlphaFoldDB; A1JMM2; -.
DR   SMR; A1JMM2; -.
DR   STRING; 393305.YE1556; -.
DR   EnsemblBacteria; CAL11634; CAL11634; YE1556.
DR   KEGG; yen:YE1556; -.
DR   PATRIC; fig|393305.7.peg.1684; -.
DR   eggNOG; COG3096; Bacteria.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.3500; -; 1.
DR   HAMAP; MF_01800; MukB; 1.
DR   InterPro; IPR012090; MukB.
DR   InterPro; IPR032520; MukB_hinge.
DR   InterPro; IPR042501; MukB_hinge_sf.
DR   InterPro; IPR007406; MukB_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF04310; MukB; 1.
DR   Pfam; PF16330; MukB_hinge; 1.
DR   PIRSF; PIRSF005246; MukB; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Chromosome partition; Coiled coil;
KW   Cytoplasm; DNA condensation; DNA-binding; Nucleotide-binding.
FT   CHAIN           1..1481
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_1000069917"
FT   REGION          666..783
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          338..480
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          509..604
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          780..805
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          835..1116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1210..1265
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ   SEQUENCE   1481 AA;  169264 MW;  785A010A04BFBC7A CRC64;
     MIERGKFRSL TLVNWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LRAGVCYSTL DVVNSRHQRV IVGVRLQQVA GRDRKVDIKP
     FTIQGLPTAI QPTQILTEVV GERQARVLSL QELKESVEAM EGVQFKQFNS ITDYHSLMFD
     LGVIPKRLRS SADRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
     ENRMTLEAIR VTQSDRDLFK HLISEATSYV AADYMRHANE RRIHLDGALV LRRELLASRK
     QLVTEQYRHV EMSRELAEQS GAESDLETDY QAASDHLSLV QTAMRQQEKI ERYQSDLEEL
     TYRLEEQNEV VAEASEQQAD NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYQQAL
     QALERARALC QLPELTADNA EDWLETFQAK EQEATEALLQ LEQKLSVADA AHSQFEQAYQ
     LVVSIAGQVS RSEAWQTARE LLRDWPSQQH LAERVQPLRM RLSELEQRLR AQQDAERLLQ
     EFCKRQGQAY QPEELEELQR ELESTVEELS LSVSDAGERR MEMRQELEQI KLKIQELTAR
     APVWLAAQDA LSQLSEQSGE ALEDSRQVTE CMQQLLERER ETTVERDEVA AAKRAIDAQI
     ERLSQPSGAE DSRMIALAER FGGVLLSEIY DDVTLDDAPY FSALYGPSRH GIVVPDLSLV
     RDQLAGLEDC PEDLYLIEGD PQSFDDSVFA VEELEKAVVV KIADRQWRYS RYPEVPLFGR
     AARENRLEAL YQERDSLAER YATLSFDVQK TQRLHQAFSR FIGSHLAVAF DSDPEAEIRL
     LNTRRGEIER ALNAHEERNQ QQRQQFEQAK EGISALNRLI PLVSLLLDDT LADRVEEITE
     ELTEAQEAAR HIQKHGASLT KLEPLLAVLQ SDPQQHEQLK ENYAQAQNSQ RQAKQQAFAL
     VEVVQRRAHF GYTDSAGMLT ENSDLNDKLR QRLEQAEAER TRAREQLRQY QAQFTQYNQV
     LASLKSSYDA KRDMLKELSQ ELVDIGVQAD ANAEARARTR RDELHAALST NRSRRNQLEK
     QLTFCEAEMD SLQKKLRKLE RDYHQIREQV VNAKAGWCAV MRMVKDNGVE RRLHRRELAY
     MDGDELRSMS DKALGALRLA VADNEHLRDV LRMSEDPKRP ERKIQFYIAV YQHLRERIRQ
     DIIRTDDPVE AIEQMEIELG RLTEELTARE QKLAISSKSV SNIIRKTIQR EQNRIRMLNQ
     GLQAVSFGQV KSVRLNVNVR EAHATLLDVL SEQQEQHQDL FNSNRLTFSE ALAKLYQRLN
     PQMDMGQRLP QTIGEELLDY RNYLELEVEV NRGADGWLRA ESGALSTGEA IGTGMSILVM
     VVQSWEEESR RLRGKDISPC RLLFLDEAAR LDAKSIATLF ELCERLEMQL IIAAPENISP
     EKGTTYKLVR KVFQNHEHVH VVGLRGFANE IPTLPSIPVE Q